|Title||Structural principles controlling HIV envelope glycosylation.|
|Publication Type||Journal Article|
|Year of Publication||2017|
|Authors||Behrens A-J, Crispin M|
|Journal||Curr Opin Struct Biol|
The heavily glycosylated, trimeric HIV-1 envelope (Env) protein is the sole viral protein exposed on the HIV-1 virion surface and is thus a main focus of antibody-mediated vaccine development. Dense glycosylation at the outer domain of Env constrains normal enzymatic processing, stalling the glycans at immature oligomannose-type structures. Furthermore, native trimerization imposes additional steric constraints, which generate an extensive 'trimer-induced mannose patch'. Importantly, the immature glycans present a highly conserved feature of the virus that is targeted by broadly neutralizing antibodies. Quantitative mass spectrometry of glycopeptides together with structures of the trimeric viral-spike define the steric principles controlling processing and provide a detailed map of the glycan shield.
|Alternate Journal||Curr. Opin. Struct. Biol.|
|PubMed Central ID||PMC5513759|
Structural principles controlling HIV envelope glycosylation.